Characterizing proteins by “ultra-fast” rotation about the magic angle
In the publication by the group around Prof. Dr. Rasmus Linser, focusing on development and application of innovative NMR-spectroscopic methodology, the authors demonstrate a further step ahead for solid-state NMR in the direction of more universal applicability. Whereas a decade ago protein amounts of 30-50 mg were necessary, a reduction by an order of magnitude was achieved over the last years due to faster rotation about the “magic angle”. Complete deuteration of the protein was, however, necessary, which was a preparative challenge and excluded many potential applications. Using the newest generation of ultra-fast rotors, which can rotate with up to 110 000 times per second, deuteration becomes dispensable and required sample amounts decrease to only half a milligram. This approach, which Linser and colleagues show in their recent work, is not a compromise but in fact provides a large range of possibilities for characterizing proteins with respect to their biological function. In particular, due to the availability of side chain protons, information on protonation states in histidine side chains can be obtained in addition to structure and site-resolved dynamics.
These studies, which are financed by the DFG in the context of an Emmy-Noether program, the collaborative research framework SFB 749, and the excellence cluster CiPS-M at the LMU Munich, are currently treated as an important paper in the journal Angewandte Chemie and shown on the cover (see picture) of one of the coming issues, well visible for the community. The new possibilities of solid-state NMR will turn out useful for understanding proteins and any related processes in the human body.
- „Assessment of a large enzyme-drug complex by proton-detected solid-state NMR without deuteration“, S. K. Vasa, H. Singh, K. Grohe and R. Linser, Angew. Chem., Int. Ed., 2019, in press, DOI: 10.1002/anie.201811714